Characterization of a non-haem ferritin of the Archaeon Halobacterium salinarum, homologous to Dps (starvation-induced DNA-binding protein)

S. Reindel; C. L. Schmidt; S. Anemüller; B. F. Matzanke

doi:10.1042/BST0300713

Characterization of a non-haem ferritin of the Archaeon Halobacterium salinarum, homologous to Dps (starvation-induced DNA-binding protein)

S. Reindel, C. L. Schmidt, S. Anemüller, B. F. Matzanke^*

^*Corresponding author for this work

9 Citations (Scopus)

Abstract

An iron-rich protein was isolated from the Archaeon Halobacterium salinarum sharing a sequence identity of 35% with the starvation-induced DNA-binding protein, DpsA, of Synechecoccus sp. PCC 7942. It consists of 20 kDa subunits, forming a dodecameric structure. The protein exhibits a ferric iron loading of up to 103 Fe ions/mol of holoprotein. CD spectra are consistent with an α-helical contribution of 58%. The UV/visible spectrum provides no evidence for the presence of haem groups. This protein exhibits features of a non-haem-type bacterial ferritin although it shares only little sequence homology with non-haem bacterial ferritin.

Original language	English
Journal	Biochemical Society Transactions
Volume	30
Issue number	4
Pages (from-to)	713-715
Number of pages	3
ISSN	0300-5127
DOIs	https://doi.org/10.1042/BST0300713
Publication status	Published - 08.2002

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Academic Focus: Center for Infection and Inflammation Research (ZIEL)

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abstract = "An iron-rich protein was isolated from the Archaeon Halobacterium salinarum sharing a sequence identity of 35% with the starvation-induced DNA-binding protein, DpsA, of Synechecoccus sp. PCC 7942. It consists of 20 kDa subunits, forming a dodecameric structure. The protein exhibits a ferric iron loading of up to 103 Fe ions/mol of holoprotein. CD spectra are consistent with an α-helical contribution of 58%. The UV/visible spectrum provides no evidence for the presence of haem groups. This protein exhibits features of a non-haem-type bacterial ferritin although it shares only little sequence homology with non-haem bacterial ferritin.",

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AU - Reindel, S.

AU - Schmidt, C. L.

AU - Anemüller, S.

AU - Matzanke, B. F.

PY - 2002/8

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N2 - An iron-rich protein was isolated from the Archaeon Halobacterium salinarum sharing a sequence identity of 35% with the starvation-induced DNA-binding protein, DpsA, of Synechecoccus sp. PCC 7942. It consists of 20 kDa subunits, forming a dodecameric structure. The protein exhibits a ferric iron loading of up to 103 Fe ions/mol of holoprotein. CD spectra are consistent with an α-helical contribution of 58%. The UV/visible spectrum provides no evidence for the presence of haem groups. This protein exhibits features of a non-haem-type bacterial ferritin although it shares only little sequence homology with non-haem bacterial ferritin.

AB - An iron-rich protein was isolated from the Archaeon Halobacterium salinarum sharing a sequence identity of 35% with the starvation-induced DNA-binding protein, DpsA, of Synechecoccus sp. PCC 7942. It consists of 20 kDa subunits, forming a dodecameric structure. The protein exhibits a ferric iron loading of up to 103 Fe ions/mol of holoprotein. CD spectra are consistent with an α-helical contribution of 58%. The UV/visible spectrum provides no evidence for the presence of haem groups. This protein exhibits features of a non-haem-type bacterial ferritin although it shares only little sequence homology with non-haem bacterial ferritin.

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SN - 0300-5127

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JO - Biochemical Society Transactions

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ER -

Characterization of a non-haem ferritin of the Archaeon Halobacterium salinarum, homologous to Dps (starvation-induced DNA-binding protein)

Abstract

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